RSMG_STRMU
ID RSMG_STRMU Reviewed; 237 AA.
AC Q93D95;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=Glucose-inhibited division protein B;
GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN OrderedLocusNames=SMU_1931;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RA Tao L., Tanzer J.M.;
RT "Novel sucrose-dependent adhesion cofactors (sdc) in Streptococcus
RT mutans.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; AF397166; AAL04086.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59542.1; -; Genomic_DNA.
DR RefSeq; NP_722236.1; NC_004350.2.
DR RefSeq; WP_002262128.1; NC_004350.2.
DR AlphaFoldDB; Q93D95; -.
DR SMR; Q93D95; -.
DR STRING; 210007.SMU_1931; -.
DR PRIDE; Q93D95; -.
DR EnsemblBacteria; AAN59542; AAN59542; SMU_1931.
DR GeneID; 66818732; -.
DR KEGG; smu:SMU_1931; -.
DR PATRIC; fig|210007.7.peg.1717; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_0_2_9; -.
DR OMA; ICFPHLH; -.
DR PhylomeDB; Q93D95; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31760; PTHR31760; 1.
DR Pfam; PF02527; GidB; 1.
DR PIRSF; PIRSF003078; GidB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..237
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184339"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ SEQUENCE 237 AA; 26773 MW; 7CC13BEADEAB030C CRC64;
MTPEEFYQAL AKHHINLSAK QKEQFDLYFK LLVEWNDKIN LTAITEEKEV YLKHFYDSIA
PLLSGYIPNE SLKLLDIGAG AGFPSLPMKI IYPQLDVTII DSLNKRIKFL NLLADALELD
KVHFYHGRAE VFGQDKNFRA HFDLVTARAV ARLQVLSELT IPFLKVGGQL LALKASAADE
ELKTAQNALN LLFSQTTSSD NYQLPNGDGR NLTIITKKKE TPNKYPRKAG MPNKKPL